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Isolation and Characterization of Tissue Inhibitors of Metalloproteinases (TIMP-1 and TIMP-2) From Human Rheumatoid Synovial Fluid

Isolation and Characterization of Tissue Inhibitors of Metalloproteinases (TIMP-1 and TIMP-2) From Human Rheumatoid Synovial Fluid

A Osthues, V Knäuper, R Oberhoff, H Reinke, H Tschesche

FEBS Lett. 1992 Jan 13;296(1):16-20.

PMID: 1730286

Abstract:

The tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2 were purified to apparent homogeneity from human rheumatoid synovial fluid (HRSF). The inhibitors were isolated by dissociation of non-covalent gelatinase/TIMP complexes. TIMP-1 migrated as a single polypeptide with Mr 28,500 on SDS-PAGE, while the Mr of TIMP-2 was 21,000. The inhibitory activity was stable under heat and acid pH. N-terminal sequence data were obtained for the first 15 residues of both inhibitors and showed identity to the human fibroblast inhibitors TIMP-1 and TIMP-2. This is the first demonstration that TIMP-1 and TIMP-2 can be directly purified from human rheumatoid synovial fluid. The complex formation between the metalloproteinase inhibitors and leucocyte metalloproteinases was shown by immunoblotting.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4241304	TIMP-2, Human Rheumatoid Synovial Fibroblast			Price

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